ID A0A377R2W1_9NEIS Unreviewed; 418 AA.
AC A0A377R2W1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NADH dehydrogenase I subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NDH-1 subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
GN Name=nuoD {ECO:0000256|HAMAP-Rule:MF_01358,
GN ECO:0000313|EMBL:STR02554.1};
GN ORFNames=NCTC13336_01431 {ECO:0000313|EMBL:STR02554.1};
OS Kingella potus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=265175 {ECO:0000313|EMBL:STR02554.1, ECO:0000313|Proteomes:UP000254293};
RN [1] {ECO:0000313|EMBL:STR02554.1, ECO:0000313|Proteomes:UP000254293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13336 {ECO:0000313|EMBL:STR02554.1,
RC ECO:0000313|Proteomes:UP000254293};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01358}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01358};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC D, E, F, and G constitute the peripheral sector of the complex.
CC {ECO:0000256|HAMAP-Rule:MF_01358}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01358};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01358}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC ECO:0000256|RuleBase:RU003685}.
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DR EMBL; UGJJ01000002; STR02554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377R2W1; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000254293; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR NCBIfam; TIGR01962; NuoD; 1.
DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358};
KW Oxidoreductase {ECO:0000313|EMBL:STR02554.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000254293};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01358};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01358}.
FT DOMAIN 121..418
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 418 AA; 47457 MW; 48F5DF3D036CE1F4 CRC64;
MATKLRNYTI NFGPQHPAAH GVLRMILELE GETIVRADPH IGLLHRGTEK LAETRTYLQA
LPYMDRLDYV SMMVNEQAYC LAVERLTGTE VPIRGQYIRT MFAEVTRILN HLMGIGSHAL
DIGAMTAILY AFRDREELMD LYEAVSGARM HAAYFRPGGV YRDLPDFMPK YESSKFRNAK
VLKELNEARE GTMLDFIDAF CQRFPGRIDT LETLLTDNRI WKQRTVGIGV VTPERALQKG
FTGVMLRGSG IEWDIRKKAP YDAYANVDFD IPVGVNGDCY DRYLCRINEM RQSVRIIQQC
SDWLKHNPGP VITGDHKIAP PKRTDMKLGM EDLIHHFKLF TEGMHVPEGE VYAAVEHPKG
EFGIYMISDG ANKPYRLKIR APGFAHLQGM DEMARGHMLA DVVAIIGTQD IVFGEVDR
//